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Q54QQ0

- IMDH_DICDI

UniProt

Q54QQ0 - IMDH_DICDI

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

impdh

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.UniRule annotation

    Catalytic activityi

    Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

    Cofactori

    Potassium.UniRule annotation

    Enzyme regulationi

    Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi329 – 3291Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi331 – 3311Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei332 – 3321IMPUniRule annotation
    Active sitei334 – 3341Thioimidate intermediateUniRule annotation
    Metal bindingi334 – 3341Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei442 – 4421IMPUniRule annotation
    Metal bindingi501 – 5011Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi502 – 5021Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi277 – 2793NADUniRule annotation
    Nucleotide bindingi327 – 3293NADUniRule annotation

    GO - Molecular functioni

    1. adenyl nucleotide binding Source: InterPro
    2. IMP dehydrogenase activity Source: dictyBase
    3. metal ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. GMP biosynthetic process Source: UniProtKB-HAMAP
    2. GTP biosynthetic process Source: dictyBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Potassium

    Enzyme and pathway databases

    UniPathwayiUPA00601; UER00295.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenaseUniRule annotation
    Short name:
    IMPDUniRule annotation
    Short name:
    IMPDHUniRule annotation
    Gene namesi
    Name:impdh
    Synonyms:guaB
    ORF Names:DDB_G0283701
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 4, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0283701. guaB.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: dictyBase
    2. phagocytic vesicle Source: dictyBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 515515Inosine-5'-monophosphate dehydrogenasePRO_0000328152Add
    BLAST

    Proteomic databases

    PRIDEiQ54QQ0.

    Expressioni

    Inductioni

    Down-regulated by Legionella pneumophila infection.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi44689.DDB_0230098.

    Structurei

    3D structure databases

    ProteinModelPortaliQ54QQ0.
    SMRiQ54QQ0. Positions 231-514.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini120 – 17960CBS 1UniRule annotationAdd
    BLAST
    Domaini183 – 23957CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni367 – 3693IMP bindingUniRule annotation
    Regioni390 – 3912IMP bindingUniRule annotation
    Regioni414 – 4185IMP bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.UniRule annotation
    Contains 2 CBS domains.UniRule annotation

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    eggNOGiCOG0517.
    KOiK00088.
    OMAiFPEYEIT.
    PhylomeDBiQ54QQ0.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH.
    InterProiIPR013785. Aldolase_TIM.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view]
    PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
    PfamiPF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000130. IMPDH. 1 hit.
    SMARTiSM00116. CBS. 2 hits.
    [Graphical view]
    TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
    PROSITEiPS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q54QQ0-1 [UniParc]FASTAAdd to Basket

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    MEKINKILQG TNSEYKSEWF VDGFDCFELF QQRHGYTYDD LIMLPGHINF    50
    SADDVSLKTK LTKNISLNAP LVSSPMDTVT EHLMAINMAL LGGIGIIHYN 100
    NTVEEQVVEV KKVKRFKNGF ITDPIVLSPT HKLSDVDMIK QKYGFSGIPI 150
    TDTGRIGGKL VGIVTSRDTD FIKDRSTTLS EVMTTDLITG QQNCTLEEAN 200
    SILKSCKKGK LPIVNDKGEL VALASRDDLV KNRDFPMATK DHENKKLLVG 250
    AALGTRETDK ERLAALSDAG VDVVILDSSQ GDSTYQREMI RFIKRNYPKI 300
    DVIGGNVVTT SQCESLIQAG VDGLRVGMGV GSICTTQEVM ACGRPQATAV 350
    FKCALYSSQY NVPIIADGGI RTIGHIIKGL SLGASSVMMG SMLAGTEEAP 400
    GDYFYKDGMR LKKYRGMGSL EAMVKGGDQR YFSETDKIKV AQGVSGSVVD 450
    KGSVKKFVPY LIQGIKHGLQ DLGCNSVTNL RESVYGGKVR FEVRTAAAQV 500
    EGSVHSLFSY EKHFI 515
    Length:515
    Mass (Da):56,311
    Last modified:May 24, 2005 - v1
    Checksum:i054EFBD2EB940868
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000056 Genomic DNA. Translation: EAL65617.1.
    RefSeqiXP_638973.1. XM_633881.1.

    Genome annotation databases

    EnsemblProtistsiDDB0230098; DDB0230098; DDB_G0283701.
    GeneIDi8624219.
    KEGGiddi:DDB_G0283701.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000056 Genomic DNA. Translation: EAL65617.1 .
    RefSeqi XP_638973.1. XM_633881.1.

    3D structure databases

    ProteinModelPortali Q54QQ0.
    SMRi Q54QQ0. Positions 231-514.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0230098.

    Proteomic databases

    PRIDEi Q54QQ0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0230098 ; DDB0230098 ; DDB_G0283701 .
    GeneIDi 8624219.
    KEGGi ddi:DDB_G0283701.

    Organism-specific databases

    dictyBasei DDB_G0283701. guaB.

    Phylogenomic databases

    eggNOGi COG0517.
    KOi K00088.
    OMAi FPEYEIT.
    PhylomeDBi Q54QQ0.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .

    Miscellaneous databases

    PROi Q54QQ0.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01964. IMPDH.
    InterProi IPR013785. Aldolase_TIM.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view ]
    PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
    Pfami PF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000130. IMPDH. 1 hit.
    SMARTi SM00116. CBS. 2 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
    PROSITEi PS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    2. Bienvenut W.V., Veltman D.M., Insall R.H.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 118-132; 143-155; 247-256 AND 431-455, IDENTIFICATION BY MASS SPECTROMETRY.
    3. "Dictyostelium transcriptional host cell response upon infection with Legionella."
      Farbrother P., Wagner C., Na J., Tunggal B., Morio T., Urushihara H., Tanaka Y., Schleicher M., Steinert M., Eichinger L.
      Cell. Microbiol. 8:438-456(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiIMDH_DICDI
    AccessioniPrimary (citable) accession number: Q54QQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3